Enzymic browning in apricots (Prunus armeniaca)
- 1 January 1991
- journal article
- research article
- Published by Wiley in Journal of the Science of Food and Agriculture
- Vol. 54 (2) , 229-234
- https://doi.org/10.1002/jsfa.2740540208
Abstract
Enzymic browning in apricots (Prunus armeniaca L) was found to be catalysed by a catechol oxidase (o‐diphenol oxidase) and a laccase (p‐diphenol oxidase), both acting on catechin and chlorogenic acid as the natural substrates. The laccase was identified as such by substrate specificity tests and the effects of selective inhibitors. The enzymes were tightly bound to the fruit tissue and were inactivated by holding at 80°C for 10 min. The levels of phenolic compounds in healthy and rotted apricot tissue were compared by paper chromatography; the levels of catechin and chlorogenic acid were reduced in the rotted tissue.Keywords
This publication has 15 references indexed in Scilit:
- The selective inhibition of catechol oxidases by salicylhydroxamic acid.Phytochemistry, 1988
- Polyphenol oxidases and peroxidases in fruits and vegetablesC R C Critical Reviews in Food Science and Nutrition, 1981
- Polyphenol oxidases in plantsPhytochemistry, 1979
- The direct linear plot. A new graphical procedure for estimating enzyme kinetic parametersBiochemical Journal, 1974
- The use of a fungal pectate lyase in the purification of laccase from peachesPhytochemistry, 1970
- A laccase-like enzyme in peachesPhytochemistry, 1968
- Polyphenolic Compounds in Canned ApricotsJournal of Food Science, 1965
- Studies on the Enzymic Browning of Apples II. Properties of Apple PolyphenoloxidaseAustralian Journal of Biological Sciences, 1964
- Latent phenolase in extracts of broad-bean (Vicia faba L.) leaves. 2. Activation by anionic wetting agentsBiochemical Journal, 1958
- Latent phenolase in extracts of broad-bean (Vicia faba L.) leaves. Activation by acid and alkaliBiochemical Journal, 1957